高等学校化学学报 ›› 2001, Vol. 22 ›› Issue (9): 1526.

• 研究论文 • 上一篇    下一篇

微乳液中脂肪酶和含明胶的微乳液凝胶中固定化脂肪酶的催化特性

周国伟, 李干佐, 黄锡荣, 徐健, 何宏娟, 李传光   

  1. 山东大学胶体与界面化学教育部重点实验室, 济南 250100
  • 收稿日期:2000-06-27 出版日期:2001-09-24 发布日期:2001-09-24
  • 通讯作者: 李干佐(1938年出生),男,教授,博士生导师,从事表面活性剂缔合结构的研究.E-mail:coliw@sdu.edu.cn E-mail:coliw@sdu.edu.cn
  • 基金资助:

    国家自然科学基金(批准号:29903006)资助

Catalytic Behavior of Lipase in W/O Microemulsion and Immobilized Lipase in Gelatin Microemulsion-Based Organogels

ZHOU Guo-Wei, LI Gan-Zuo, HUANG Xi-Rong, XU Jian, HE Hong-Juan, LI Chuan-Guang   

  1. Key Laboratory for Colloid and Interface Chemistry of State Educational Ministry, Shandong University, Jinan 250100, China
  • Received:2000-06-27 Online:2001-09-24 Published:2001-09-24

摘要: 在双2-乙基己基琥珀酸酯磺酸钠(AOT)油包水微乳液中Calytical脂肪酶催化月桂酸和戊醇的酯化反应动力学研究表明,反应符合乒乓(BiBi)机制.表观速率常数km酸=0.13518mol/L,km醇=0.22423mol/L,最大反应速度vmax=1.3873×10-5mol/(L·min·mg).将该脂肪酶固定于含明胶的微乳液凝胶(MBGs)中,制得固定化脂肪酶,含酶MBGs在非极性溶剂中可作为固相催化剂,并研究了其在辛烷中催化酯化的性能.所制得的含酶MBGs物理稳定性好,重复利用10次以上,其转化率仍达初始转化率的90%.

关键词: 油包水微乳液, 酶催化, 固定化酶, 微乳液凝胶, 动力学

Abstract: The kinetics of the esterification of lauric acid and 1 pentanol catalyzed by Calytical (CL) lipase, was studied in water/bis (2-ethylhexyl)sulfosuccinate sodium(AOT)/isooctane microemulsions. The kinetics studies showed that the reaction followed a Ping Pong Bi-Bi mechanism. The values of all apparent kinetic parameters were determined. The apparent kinetic parameters of the reaction were found to be km(lauric acid)=013518 mol/L, km(1 pentanol)=022423 mol/Land vmax=13873×10-5 mol/(L·min·mg). Lipase has also been immobilized in gelatin containing AOT-microemulsion based organogels(MBGs). These lipase containing MBGs prove to be a novel solid-phase catalysts for the use in apolar organic solvents and have a good physical stability. These lipase containing MBGs retained its higher activity after 10 runs esterification reactions.

Key words: W/O microemulsion, Enzyme catalysis, Immobilized enzyme, Microemulsion based gels, Kinetics

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